CONFORMATIONAL PREFERENCES OF OLIGOPEPTIDES RICH IN ALPHA-AMINOISOBUTYRIC-ACID .1. OBSERVATION OF A 3(10)/ALPHA-HELICAL TRANSITION UPON SEQUENCE PERMUTATION

被引：57

作者：

BASU, G

BAGCHI, K

KUKI, A

机构：

[1] Cornell University, Department of Chemistry, Baker Laboratory, Ithaca, New York

来源：

BIOPOLYMERS | 1991年 / 31卷 / 14期

关键词：

D O I：

10.1002/bip.360311410

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The solution conformation of peptides rich in the alpha,alpha-dialkylated amino acid Aib has proven to be a subtle problem, not because of helix/coil transitions, but rather because of alpha-helical/3(10)-helical competition. A special series of peptides containing 75% Aib has been synthesized that feature identical amino acid composition but differing sequences; they are sequence permutation isomers. Nuclear magnetic resonance hydrogen-bonding studies reveal that there is a sequence permutation induced transition between the two alternative helical forms within this set. The implications for the design and conformational prediction of helical Aib-rich peptides are discussed.

引用

页码：1763 / 1774

页数：12

共 34 条

[1] STEREOCHEMISTRY OF ALPHA-AMINOISOBUTYRIC-ACID PEPTIDES IN SOLUTION - CONFORMATIONS OF DECAPEPTIDES WITH A CENTRAL TRIPLET OF CONTIGUOUS L-AMINO-ACIDS [J].